Antibody-like Protein via Ferritin Self-Assembly
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Solution Overview
Problem
Current target-oriented drug delivery systems face limitations in antigen binding specificity and immune response induction due to the size and structure of antibodies, which restricts their efficacy and applicability.
Innovation Solution
Development of an antibody-like protein composed of self-assembled ferritin monomers fused with complementarity determining regions (CDRs), allowing for high-density antigen binding and reduced immune response by using only the CDRs, enabling simultaneous binding to multiple antigens with enhanced avidity.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If an entire antibody is used for antigen binding, then antigen binding capability is achieved, but unnecessary immune response is induced and production/storage complexity increases
Solution Approach 1:
The patent extracts only the complementarity determining regions (CDRs) from the full antibody structure and fuses them to ferritin monomers. This extraction approach retains the essential antigen-binding function while eliminating the unnecessary parts of the antibody that would otherwise induce immune responses. The CDRs are the minimal functional units required for antigen recognition, making this an optimal extraction strategy.
Solution Approach 2:
The antibody structure is segmented into functional components: the CDRs (responsible for antigen binding) and the rest of the antibody structure (which can induce immune responses). By separating these components and using only the CDRs in the fusion protein, the patent achieves functional specificity while reducing harmful immune reactions.
2Reliability
If an entire antibody is used for antigen binding, then antigen binding capability is achieved, but production and storage difficulty increases
Solution Approach 1:
By extracting only the CDRs from the full antibody, the patent creates a smaller, simpler protein structure that is easier to produce and store. The CDRs are shorter peptide sequences compared to full antibodies, reducing the complexity of protein folding, purification, and storage requirements.
Solution Approach 2:
The patent creates a composite protein structure by fusing CDRs with ferritin monomers. This composite approach combines the antigen-binding functionality of CDRs with the structural stability and ease of handling properties of ferritin, resulting in a protein that is both functional and easy to manufacture and store.
3Reliability
If conventional antibodies are used, then antigen binding is achieved with limited specificity, but the large size and structure restrict efficacy and applicability
Solution Approach 1:
The patent segments the antibody structure to use only the CDRs, which are the minimal units for antigen binding. This segmentation allows for greater flexibility in designing antibodies against different antigens while maintaining high specificity, as the CDRs can be optimized for each target without being constrained by the fixed structure of full antibodies.
Solution Approach 2:
By changing the size parameter of the antigen-binding unit from full antibody (large) to CDR fragment (small), the patent enables better penetration into target tissues and cells. The reduced size improves pharmacokinetics and allows the protein to access harder-to-reach targets while maintaining binding specificity through the preserved CDR sequences.
Applied Scientific Principles
This section explains which scientific principles are used to turn an abstract innovation direction into a practical engineering solution.
Function Achieved in This Case
The antibody-like protein achieves improved antigen binding affinity and reduced immune response, facilitating effective drug delivery and disease treatment with enhanced therapeutic efficacy and ease of production and storage.
Implementation Method 1
an antibody-like protein including self-assembly of a plurality of ferritin monomers
Data Source
AI summary
An antibody-like protein is formed by self-assembly of a plurality of ferritin monomers including at least CDR-ferritin monomers having a complementarity-determining region of an antibody fused thereto whereby the antibody-like protein has the complementarity-determining regions present at a high density on the surface or outside thereof so that even some of the complementarity-determining regions, such as HCDR3, etc., can bind to an antigen at an affinity level similar to that of the antibody, and the antibody-like protein possesses a structural feature advantageous for binding simultaneously to a plurality of antigens, and as such, has remarkably improved binding avidity, compared to the antibody. The antibody-like protein of the present invention is an antibody substitute that can be utilized in antibody-based uses and fields.